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PID/WAG 介导的拟南芥 PIN3 生长素转运体磷酸化在向重力性过程中调节极性转换。

PID/WAG-mediated phosphorylation of the Arabidopsis PIN3 auxin transporter mediates polarity switches during gravitropism.

机构信息

Institute of Science and Technology Austria (IST Austria), Am Campus 1, 3400, Klosterneuburg, Austria.

Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences (BOKU), Muthgasse 18, 1190, Vienna, Austria.

出版信息

Sci Rep. 2018 Jul 6;8(1):10279. doi: 10.1038/s41598-018-28188-1.

Abstract

Intercellular distribution of the plant hormone auxin largely depends on the polar subcellular distribution of the plasma membrane PIN-FORMED (PIN) auxin transporters. PIN polarity switches in response to different developmental and environmental signals have been shown to redirect auxin fluxes mediating certain developmental responses. PIN phosphorylation at different sites and by different kinases is crucial for PIN function. Here we investigate the role of PIN phosphorylation during gravitropic response. Loss- and gain-of-function mutants in PINOID and related kinases but not in D6PK kinase as well as mutations mimicking constitutive dephosphorylated or phosphorylated status of two clusters of predicted phosphorylation sites partially disrupted PIN3 phosphorylation and caused defects in gravitropic bending in roots and hypocotyls. In particular, they impacted PIN3 polarity rearrangements in response to gravity and during feed-back regulation by auxin itself. Thus PIN phosphorylation, besides regulating transport activity and apical-basal targeting, is also important for the rapid polarity switches in response to environmental and endogenous signals.

摘要

细胞间生长素的分布在很大程度上取决于质膜 PIN 形成(PIN)生长素转运蛋白的极性亚细胞分布。已经表明,PIN 极性在响应不同的发育和环境信号时发生转换,从而重新引导介导某些发育反应的生长素流。不同位点和不同激酶的 PIN 磷酸化对于 PIN 功能至关重要。在这里,我们研究了 PIN 磷酸化在向重力性反应中的作用。PIN 同源性和相关激酶的缺失和功能获得突变体,但 D6PK 激酶的缺失和功能获得突变体除外,以及模拟两个预测磷酸化位点簇的组成性去磷酸化或磷酸化状态的突变体部分破坏了 PIN3 的磷酸化,并导致根和下胚轴的向重力弯曲缺陷。特别是,它们影响了 PIN3 在重力响应和生长素自身反馈调节过程中的极性重排。因此,除了调节运输活性和顶端-基底靶向外,PIN 磷酸化对于快速响应环境和内源性信号的极性转换也很重要。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3a4c/6035267/d61081993465/41598_2018_28188_Fig1_HTML.jpg

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